1wlg



Crystal structure of FlgE31, a major fragment of the hook protein

Overview
The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.

Other Views
A single chain.

About this Structure
1WLG is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference
Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism., Samatey FA, Matsunami H, Imada K, Nagashima S, Shaikh TR, Thomas DR, Chen JZ, Derosier DJ, Kitao A, Namba K, Nature. 2004 Oct 28;431(7012):1062-8. PMID:15510139

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